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Conserved domains on  [gi|1720372925|ref|XP_030102765|]
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inverted formin-2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FH2 super family cl19758
Formin Homology 2 Domain;
587-951 3.42e-76

Formin Homology 2 Domain;


The actual alignment was detected with superfamily member pfam02181:

Pssm-ID: 418645  Cd Length: 372  Bit Score: 257.20  E-value: 3.42e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  587 HRRVNPPTLRMKKLNWQKLpsNVARERNSMWATLGSPcTAAVEPDFSSIEQLFSfptAKPKEPSAAP------ARKEPKE 660
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKV--RPSQDRGTVWDKLDDE-SFELDGDLSELEELFS---AKAKTKKNKKsedkssSKKKPKE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  661 VTFLDSKKSLNLNIFLKQFKCSNEEVTSMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLSNADQFYVLLL 740
Cdd:pfam02181   75 VSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  741 DIPCYPLRVECMmlcegtAIVLD------MVRPKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKIS 814
Cdd:pfam02181  155 KIPRLEARLRAL------LFKSTfeeeieELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  815 TLLKLTETKSQQSRVTLLHHVLEEVEKSHPDLLQLSRDLEPPSQAAGINVEIIHSEASA------NLKKLLEAERKVSAS 888
Cdd:pfam02181  229 SLLKLSDTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQlerglkKLERELELSALDEHP 308
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720372925  889 IPEVQKQYAERLQASIEASQELDKVFDAIEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLF 951
Cdd:pfam02181  309 DDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
156-341 3.27e-43

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


:

Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 155.89  E-value: 3.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  156 EGHALTLDALDHYKMVCSQQYRFSVIMSELSD--SDNVPYVVTLLSVINAIILGPEDLRSRAQLRSEFIGLQLLDILTRL 233
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSseNDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  234 RDLEDADLLIQLEAFEEAKAEDEEELQRISD--GINMNSHQEVFASLFHKVSCSPASAQLLSVLQGLMHLEPAGRSGQLL 311
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDdvNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720372925  312 WEALENLVNRAVLLAS-----DAQACTLEEVVERL 341
Cdd:pfam06367  161 WKLLEELVSQIVLHRTkpdpkFDERKNLEIDINRL 195
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
8-152 9.25e-16

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


The actual alignment was detected with superfamily member pfam06371:

Pssm-ID: 461886  Cd Length: 188  Bit Score: 76.97  E-value: 9.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925    8 QRKWAALKEKLGPQDSDptEANLESAEPELCIRLLQM-PSVVNY-SGLRKRLESSDGGWMVQFLEQSGLDLLLEALARLS 85
Cdd:pfam06371   44 QYKSTNFQKEGGGSKSD--SESNETGSPEYYVKKLKDdSISSKQlESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKIN 121
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720372925   86 GRGVARISDALLQLTCISCVRAVMNSQQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCI 152
Cdd:pfam06371  122 RKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
WH2_INF2 cd22061
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
997-1026 5.27e-15

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).


:

Pssm-ID: 409204  Cd Length: 30  Bit Score: 69.87  E-value: 5.27e-15
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720372925  997 KQEEVCVIDALLADIRKGFQLRKTARGRGD 1026
Cdd:cd22061      1 KQEEVCVIDALLADIRKGFQLRKTARGRGD 30
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
1034-1278 2.61e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.01  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1034 APADPPKATEPATASNPTQGTNHPASEPLDTTAADEPQgwdlvDAVTPSPQPSKE-------EDGPPALERRSSWYVDAI 1106
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPE-----ETARAPSSPPAEpppstppAAASPRPPRRSSPISASA 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1107 DFLDPEDTPDAQPSEGVWPVTLGDGQALNPLEFSSNKPPgvKSSHQDATDPEALWGVHRTEADSTSEGPEDEAQRGQSTH 1186
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP--LPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1187 lPRTGPGEDEDGEDTAPESAldtSLDRSFSEDAVTDSSGSGTLPRVQGRVSKGTSKRRKKRPSRnqeGPGTSPCCPAGPS 1266
Cdd:PHA03307   296 -PSPSPSSPGSGPAPSSPRA---SSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSR---PPPPADPSSPRKR 368
                          250
                   ....*....|..
gi 1720372925 1267 LTPAGPTGSTSI 1278
Cdd:PHA03307   369 PRPSRAPSSPAA 380
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
587-951 3.42e-76

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 257.20  E-value: 3.42e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  587 HRRVNPPTLRMKKLNWQKLpsNVARERNSMWATLGSPcTAAVEPDFSSIEQLFSfptAKPKEPSAAP------ARKEPKE 660
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKV--RPSQDRGTVWDKLDDE-SFELDGDLSELEELFS---AKAKTKKNKKsedkssSKKKPKE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  661 VTFLDSKKSLNLNIFLKQFKCSNEEVTSMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLSNADQFYVLLL 740
Cdd:pfam02181   75 VSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  741 DIPCYPLRVECMmlcegtAIVLD------MVRPKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKIS 814
Cdd:pfam02181  155 KIPRLEARLRAL------LFKSTfeeeieELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  815 TLLKLTETKSQQSRVTLLHHVLEEVEKSHPDLLQLSRDLEPPSQAAGINVEIIHSEASA------NLKKLLEAERKVSAS 888
Cdd:pfam02181  229 SLLKLSDTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQlerglkKLERELELSALDEHP 308
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720372925  889 IPEVQKQYAERLQASIEASQELDKVFDAIEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLF 951
Cdd:pfam02181  309 DDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
590-984 4.57e-60

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 211.83  E-value: 4.57e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925   590 VNPPTLRMKKLNWQKLpsNVARERNSMWATLGSPctaaVEPDFSSIEQLFSfptAKPKEPSAAPARKEPK---------E 660
Cdd:smart00498    3 EPKPKKKLKPLHWDKL--NPSDLSGTVWDKIDEE----SEGDLDELEELFS---AKEKTKSASKDVSEKKsilkkkasqE 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925   661 VTFLDSKKSLNLNIFLKQFKCSNEEVTSMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERA-KLSNADQFYVLL 739
Cdd:smart00498   74 FKILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPeELARAEQFLLLI 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925   740 LDIPCYPLRVECMMLcegTAIVLDMVR---PKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKISTL 816
Cdd:smart00498  154 SNIPYLEERLNALLF---KANFEEEVEdlkPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSL 230
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925   817 LKLTETKSQQSRVTLLHHVLEEVEKSHpdllqlSRDLEPPSQAaginveiiHSEASAnlkklleaerKVSASIPEVQKQY 896
Cdd:smart00498  231 LKLSDVKSADNKTTLLHFLVKIIRKKY------LGGLSDPENL--------DDKFIE----------VMKPFLKAAKEKY 286
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925   897 aerlqasieasQELDKVFDAIEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLFTRALKENKDRKEQMakaERRKQQLA 976
Cdd:smart00498  287 -----------DKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEE---EERRKKLV 352

                    ....*...
gi 1720372925   977 EEEARRPR 984
Cdd:smart00498  353 KETTEYEQ 360
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
156-341 3.27e-43

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 155.89  E-value: 3.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  156 EGHALTLDALDHYKMVCSQQYRFSVIMSELSD--SDNVPYVVTLLSVINAIILGPEDLRSRAQLRSEFIGLQLLDILTRL 233
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSseNDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  234 RDLEDADLLIQLEAFEEAKAEDEEELQRISD--GINMNSHQEVFASLFHKVSCSPASAQLLSVLQGLMHLEPAGRSGQLL 311
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDdvNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720372925  312 WEALENLVNRAVLLAS-----DAQACTLEEVVERL 341
Cdd:pfam06367  161 WKLLEELVSQIVLHRTkpdpkFDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
8-152 9.25e-16

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 76.97  E-value: 9.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925    8 QRKWAALKEKLGPQDSDptEANLESAEPELCIRLLQM-PSVVNY-SGLRKRLESSDGGWMVQFLEQSGLDLLLEALARLS 85
Cdd:pfam06371   44 QYKSTNFQKEGGGSKSD--SESNETGSPEYYVKKLKDdSISSKQlESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKIN 121
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720372925   86 GRGVARISDALLQLTCISCVRAVMNSQQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCI 152
Cdd:pfam06371  122 RKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
WH2_INF2 cd22061
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
997-1026 5.27e-15

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).


Pssm-ID: 409204  Cd Length: 30  Bit Score: 69.87  E-value: 5.27e-15
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720372925  997 KQEEVCVIDALLADIRKGFQLRKTARGRGD 1026
Cdd:cd22061      1 KQEEVCVIDALLADIRKGFQLRKTARGRGD 30
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1034-1278 2.61e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.01  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1034 APADPPKATEPATASNPTQGTNHPASEPLDTTAADEPQgwdlvDAVTPSPQPSKE-------EDGPPALERRSSWYVDAI 1106
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPE-----ETARAPSSPPAEpppstppAAASPRPPRRSSPISASA 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1107 DFLDPEDTPDAQPSEGVWPVTLGDGQALNPLEFSSNKPPgvKSSHQDATDPEALWGVHRTEADSTSEGPEDEAQRGQSTH 1186
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP--LPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1187 lPRTGPGEDEDGEDTAPESAldtSLDRSFSEDAVTDSSGSGTLPRVQGRVSKGTSKRRKKRPSRnqeGPGTSPCCPAGPS 1266
Cdd:PHA03307   296 -PSPSPSSPGSGPAPSSPRA---SSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSR---PPPPADPSSPRKR 368
                          250
                   ....*....|..
gi 1720372925 1267 LTPAGPTGSTSI 1278
Cdd:PHA03307   369 PRPSRAPSSPAA 380
WH2 smart00246
Wiskott Aldrich syndrome homology region 2; Wiskott Aldrich syndrome homology region 2 / ...
1005-1020 8.21e-03

Wiskott Aldrich syndrome homology region 2; Wiskott Aldrich syndrome homology region 2 / actin-binding motif


Pssm-ID: 128542  Cd Length: 18  Bit Score: 34.87  E-value: 8.21e-03
                            10
                    ....*....|....*.
gi 1720372925  1005 DALLADIRKGFQLRKT 1020
Cdd:smart00246    3 SALLAQIRQGKKLKKV 18
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
836-994 9.16e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 9.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  836 LEEVEKSHPDLLQLSRDLEppsqaaginveiIHSEASANLKKLLEAERKVsASIPEVQKQYAERLQASIEASQELDKVFD 915
Cdd:COG4717    104 LEELEAELEELREELEKLE------------KLLQLLPLYQELEALEAEL-AELPERLEELEERLEELRELEEELEELEA 170
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720372925  916 AIEQKKLELADyLCEDPQQLSLEDTFSTMKTFRDLFTRALKENKDRKEQMAKAERRKQQLAEEEARRPRDEDGKPIRKG 994
Cdd:COG4717    171 ELAELQEELEE-LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
587-951 3.42e-76

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 257.20  E-value: 3.42e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  587 HRRVNPPTLRMKKLNWQKLpsNVARERNSMWATLGSPcTAAVEPDFSSIEQLFSfptAKPKEPSAAP------ARKEPKE 660
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKV--RPSQDRGTVWDKLDDE-SFELDGDLSELEELFS---AKAKTKKNKKsedkssSKKKPKE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  661 VTFLDSKKSLNLNIFLKQFKCSNEEVTSMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLSNADQFYVLLL 740
Cdd:pfam02181   75 VSLLDPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  741 DIPCYPLRVECMmlcegtAIVLD------MVRPKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKIS 814
Cdd:pfam02181  155 KIPRLEARLRAL------LFKSTfeeeieELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  815 TLLKLTETKSQQSRVTLLHHVLEEVEKSHPDLLQLSRDLEPPSQAAGINVEIIHSEASA------NLKKLLEAERKVSAS 888
Cdd:pfam02181  229 SLLKLSDTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQlerglkKLERELELSALDEHP 308
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720372925  889 IPEVQKQYAERLQASIEASQELDKVFDAIEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLF 951
Cdd:pfam02181  309 DDKFREVLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
590-984 4.57e-60

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 211.83  E-value: 4.57e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925   590 VNPPTLRMKKLNWQKLpsNVARERNSMWATLGSPctaaVEPDFSSIEQLFSfptAKPKEPSAAPARKEPK---------E 660
Cdd:smart00498    3 EPKPKKKLKPLHWDKL--NPSDLSGTVWDKIDEE----SEGDLDELEELFS---AKEKTKSASKDVSEKKsilkkkasqE 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925   661 VTFLDSKKSLNLNIFLKQFKCSNEEVTSMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERA-KLSNADQFYVLL 739
Cdd:smart00498   74 FKILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEDPeELARAEQFLLLI 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925   740 LDIPCYPLRVECMMLcegTAIVLDMVR---PKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKISTL 816
Cdd:smart00498  154 SNIPYLEERLNALLF---KANFEEEVEdlkPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSL 230
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925   817 LKLTETKSQQSRVTLLHHVLEEVEKSHpdllqlSRDLEPPSQAaginveiiHSEASAnlkklleaerKVSASIPEVQKQY 896
Cdd:smart00498  231 LKLSDVKSADNKTTLLHFLVKIIRKKY------LGGLSDPENL--------DDKFIE----------VMKPFLKAAKEKY 286
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925   897 aerlqasieasQELDKVFDAIEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLFTRALKENKDRKEQMakaERRKQQLA 976
Cdd:smart00498  287 -----------DKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEE---EERRKKLV 352

                    ....*...
gi 1720372925   977 EEEARRPR 984
Cdd:smart00498  353 KETTEYEQ 360
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
156-341 3.27e-43

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 155.89  E-value: 3.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  156 EGHALTLDALDHYKMVCSQQYRFSVIMSELSD--SDNVPYVVTLLSVINAIILGPEDLRSRAQLRSEFIGLQLLDILTRL 233
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSseNDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  234 RDLEDADLLIQLEAFEEAKAEDEEELQRISD--GINMNSHQEVFASLFHKVSCSPASAQLLSVLQGLMHLEPAGRSGQLL 311
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDdvNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720372925  312 WEALENLVNRAVLLAS-----DAQACTLEEVVERL 341
Cdd:pfam06367  161 WKLLEELVSQIVLHRTkpdpkFDERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
8-152 9.25e-16

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 76.97  E-value: 9.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925    8 QRKWAALKEKLGPQDSDptEANLESAEPELCIRLLQM-PSVVNY-SGLRKRLESSDGGWMVQFLEQSGLDLLLEALARLS 85
Cdd:pfam06371   44 QYKSTNFQKEGGGSKSD--SESNETGSPEYYVKKLKDdSISSKQlESLRVALRTQPLSWVRRFIEAQGLGALLNVLSKIN 121
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720372925   86 GRGVARISDALLQLTCISCVRAVMNSQQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCI 152
Cdd:pfam06371  122 RKKSQEEEDLDREYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
WH2_INF2 cd22061
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This ...
997-1026 5.27e-15

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Inverted formin-2 (INF2); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in inverted formin-2 (INF2, also known as HBEBP2-binding protein C). INF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring severing of the filament. It interacts with actin at its formin homology 2 (FH2) domain, while the WH2 domain acts as the diaphanous autoregulatory domain (DAD) and binds to actin monomers. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. It accelerates actin nucleation and elongation by interacting with the fast-growing ends (barbed ends) of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth Disease (CMTD).


Pssm-ID: 409204  Cd Length: 30  Bit Score: 69.87  E-value: 5.27e-15
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720372925  997 KQEEVCVIDALLADIRKGFQLRKTARGRGD 1026
Cdd:cd22061      1 KQEEVCVIDALLADIRKGFQLRKTARGRGD 30
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1034-1278 2.61e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.01  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1034 APADPPKATEPATASNPTQGTNHPASEPLDTTAADEPQgwdlvDAVTPSPQPSKE-------EDGPPALERRSSWYVDAI 1106
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPE-----ETARAPSSPPAEpppstppAAASPRPPRRSSPISASA 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1107 DFLDPEDTPDAQPSEGVWPVTLGDGQALNPLEFSSNKPPgvKSSHQDATDPEALWGVHRTEADSTSEGPEDEAQRGQSTH 1186
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP--LPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1187 lPRTGPGEDEDGEDTAPESAldtSLDRSFSEDAVTDSSGSGTLPRVQGRVSKGTSKRRKKRPSRnqeGPGTSPCCPAGPS 1266
Cdd:PHA03307   296 -PSPSPSSPGSGPAPSSPRA---SSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSR---PPPPADPSSPRKR 368
                          250
                   ....*....|..
gi 1720372925 1267 LTPAGPTGSTSI 1278
Cdd:PHA03307   369 PRPSRAPSSPAA 380
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1026-1275 1.47e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1026 DTEASGRVAPADPPKATEPATASNPTQGTNHPASEPL----------DTTAADEPQG-WDLVDAVTPSPQPSKE-EDGPP 1093
Cdd:PHA03307   154 AAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPaepppstppaAASPRPPRRSsPISASASSPAPAPGRSaADDAG 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1094 ALERRSSWYVDAIDFLDPED-TPDAQPSEGVWPVTLGDGQALNPLEF--SSNKPPGVKSSHQDATDP------------- 1157
Cdd:PHA03307   234 ASSSDSSSSESSGCGWGPENeCPLPRPAPITLPTRIWEASGWNGPSSrpGPASSSSSPRERSPSPSPsspgsgpapsspr 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1158 --EALWGVHRTEADSTSEGPEDEAQRGqsthlPRTGPGEDEDGEDTAPESALDTSLDRsfsedavtdSSGSGTLPRVQGR 1235
Cdd:PHA03307   314 asSSSSSSRESSSSSTSSSSESSRGAA-----VSPGPSPSRSPSPSRPPPPADPSSPR---------KRPRPSRAPSSPA 379
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1720372925 1236 VSKGTSKRRKKRPS-----RNQEGPGTSPCCPAGPSLTPAGPTGS 1275
Cdd:PHA03307   380 ASAGRPTRRRARAAvagraRRRDATGRFPAGRPRPSPLDAGAASG 424
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
876-1000 5.35e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 5.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  876 KKLLEAERKVSASIPEVQKQYAERLQASIEASQELDKVfdAIEQKKLELadylcEDPQQLSLEDTFSTMKTFRDLFTRAL 955
Cdd:pfam17380  316 RKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKREL-----ERIRQEEIAMEISRMRELERLQMERQ 388
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720372925  956 KENKDRKEQMAKAerRKQQLAEEEARRPRDEDGKPIRKGPGKQEE 1000
Cdd:pfam17380  389 QKNERVRQELEAA--RKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1038-1277 2.09e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1038 PPKATEPATASNPTQGTNHPASEPLDTTAADEPqgwdLVDAVTPSPQPSKEEDGPPALERRSSwyvdAIDFLDPEDTPDA 1117
Cdd:PHA03307    94 TLAPASPAREGSPTPPGPSSPDPPPPTPPPASP----PPSPAPDLSEMLRPVGSPGPPPAASP----PAAGASPAAVASD 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1118 QPSEGVWPVTLGDGQALNPLEFSSNKPPGVKSSHQDATDPEAlwGVHRTEADSTSE-------GPEDEAQRGQSTHLPRT 1190
Cdd:PHA03307   166 AASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPP--RRSSPISASASSpapapgrSAADDAGASSSDSSSSE 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925 1191 GPGEDEDGEDTAPESaldtsldrsfsedavtdSSGSGTLPRVQGRVSKGTSKRRKKRPSRNQEGPGtSPCCPAGPSLTPA 1270
Cdd:PHA03307   244 SSGCGWGPENECPLP-----------------RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPR-ERSPSPSPSSPGS 305

                   ....*..
gi 1720372925 1271 GPTGSTS 1277
Cdd:PHA03307   306 GPAPSSP 312
WH2 smart00246
Wiskott Aldrich syndrome homology region 2; Wiskott Aldrich syndrome homology region 2 / ...
1005-1020 8.21e-03

Wiskott Aldrich syndrome homology region 2; Wiskott Aldrich syndrome homology region 2 / actin-binding motif


Pssm-ID: 128542  Cd Length: 18  Bit Score: 34.87  E-value: 8.21e-03
                            10
                    ....*....|....*.
gi 1720372925  1005 DALLADIRKGFQLRKT 1020
Cdd:smart00246    3 SALLAQIRQGKKLKKV 18
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
836-994 9.16e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 9.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720372925  836 LEEVEKSHPDLLQLSRDLEppsqaaginveiIHSEASANLKKLLEAERKVsASIPEVQKQYAERLQASIEASQELDKVFD 915
Cdd:COG4717    104 LEELEAELEELREELEKLE------------KLLQLLPLYQELEALEAEL-AELPERLEELEERLEELRELEEELEELEA 170
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720372925  916 AIEQKKLELADyLCEDPQQLSLEDTFSTMKTFRDLFTRALKENKDRKEQMAKAERRKQQLAEEEARRPRDEDGKPIRKG 994
Cdd:COG4717    171 ELAELQEELEE-LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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